3QID

Crystal structures and functional analysis of murine norovirus RNA-dependent RNA polymerase

3QID の概要

• エントリーDOI: 10.2210/pdb3qid/pdb
• 関連するPDBエントリー: 1SHO 2B43 3BSO 3H5X
• 分子名称: RNA dependent RNA polymerase, SULFATE ION, MANGANESE (III) ION, ... (5 entities in total)
• 機能のキーワード: rna polymerase, viral replication enzyme, transferase
• 由来する生物種: Murine norovirus 1
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 179334.14

構造登録者

Kim, K.H.,Intekhab, A.,Lee, J.H. (登録日: 2011-01-27, 公開日: 2011-12-21, 最終更新日: 2023-11-01)

主引用文献

Lee, J.H.,Alam, I.,Han, K.R.,Cho, S.,Shin, S.,Kang, S.,Yang, J.M.,Kim, K.H.
Crystal structures of murine norovirus-1 RNA-dependent RNA polymerase.
J.Gen.Virol., 92:1607-1616, 2011

PubMed Abstract: Norovirus is one of the leading agents of gastroenteritis and is a major public health concern. In this study, the crystal structures of recombinant RNA-dependent RNA polymerase (RdRp) from murine norovirus-1 (MNV-1) and its complex with 5-fluorouracil (5FU) were determined at 2.5 Å resolution. Crystals with C2 symmetry revealed a dimer with half a dimer in the asymmetrical unit, and the protein exists predominantly as a monomer in solution, in equilibrium with a smaller population of dimers, trimers and hexamers. MNV-1 RdRp exhibited polymerization activity with a right-hand fold typical of polynucleotide polymerases. The metal ion modelled in close proximity to the active site was found to be coordinated tetrahedrally to the carboxyl groups of aspartate clusters. The orientation of 5FU observed in three molecules in the asymmetrical unit was found to be slightly different, but it was stabilized by a network of favourable interactions with the conserved active-site residues Arg185, Asp245, Asp346, Asp347 and Arg395. The information gained on the structural and functional features of MNV-1 RdRp will be helpful in understanding replication of norovirus and in designing novel therapeutic agents against this important pathogen.

PubMed: 21471315
DOI: 10.1099/vir.0.031104-0

実験手法

X-RAY DIFFRACTION (2.5 Å)